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Figure 1.
Figure 1. The NMR solution of structures of (A) the F-spondin
TSR domain 1 and (B) the F-spondin TSR domain 4. Twenty
energy-refined conformers are shown for each domain. The first
strand has a rippled conformation, which is characteristic for
this fold. The two other strands form an antiparallel  -sheet
(residues 462-467 and 484-489 for TSR1, and 634-640 and 657-663
for TSR4). TSR1 has a short additional -sheet
in the region where TSR4 has a less well-defined loop region
(residues 443-445 and 471-473). The secondary structure and core
residues of a representative conformer of the solution
structures of the F-spondin (C) TSR1 and (D) TSR4 domains are
shown. Tryptophans are drawn in blue, arginines in red, and
cysteines in yellow. The green residue in TSR1 is tyrosine,
which may further stabilize the structure through interactions
with the nearby arginine side-chain. In TSR4, this residue is
leucine. Aspartate 485 is shown in magenta.
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